Richard Henderson from the Medical Research Council Laboratory of Molecular Biology's (LMB’s) Structural Studies Division has been awarded the Royal Society’s most prestigious award, the Copley Medal. This is the world’s oldest scientific prize, first awarded in 1731.
Richard Henderson wins Royal Society’s prestigious Copley Medal
Richard has been awarded the prize for his work on imaging techniques that have enabled scientists to understand the arrangements of atoms in important biomolecules.
Knowledge of the structures of proteins and biomolecules is vital for understanding essential processes in the body and is a key part of modern drug design – making more effective pharmaceuticals which better interact with target proteins in the body. Initially scientists could only use X-ray crystallography to determine the structure of biomolecules but this technique can’t be used with all proteins and macromolecules. Work over Richard’s career has helped to pioneer techniques using electron microscopy, which bombards proteins or other large biological molecules with electrons rather than X-rays. Richard first realised the potential of electron microscopy in the 1970s to image 2-D crystals of proteins that could not be imaged with X-ray crystallography, through a very productive collaboration with Nigel Unwin (who was awarded the Royal Society Croonian Medal in 2000). Using electron microscopy, he and his colleagues were able to determine high resolution structures of a cell membrane protein for the first time.
In the 1990s, Richard had the insight to realise that it would be theoretically possible to extract enough signal from randomly dispersed molecules using electron microscopy to obtain their detailed atomic structures. This insight and Richard’s drive and determination over the next two decades led to the development of better detectors for electron microscopes and better software to analyse the images. This revolutionised the technique of electron cryomicroscopy (cryoEM), which involves flash-cooling molecules in a thin layer of aqueous solution before imaging them, a method invented by Jacques Dubochet and his colleagues in the early 1980s. The cryoEM technique has made it possible to analyse many molecules whose structure could not be determined using X-ray crystallography and has dramatically expanded what can be done in structural biology.
In the last few years there has been a quantum step forward in these imaging techniques, due to better microscopes, better electron detectors and better computer programs for calculating the structure from the images. These improvements are now allowing atomic structure determinations of many protein and other macromolecular assemblies that were previously very difficult or impossible to obtain. The new structures provide important insights into the biological function of the assemblies and, by catalysing the subsequent development of new diagnostic or therapeutic tools, should help to improve the health and wealth of the country. The award recognises not only Richard’s own ground-breaking work in electron microscopy but also his work in advancing and disseminating his ideas to the point where they have reached fruition and are now used prolifically across the world.
The Royal Society recognises excellence in science and technology through its medals, awards and prize lectures. The Copley Medal is awarded annually “for outstanding achievements in research in any branch of science”. Previous LMB winners include Francis Crick (1975), Fred Sanger (1977), Max Perutz (1979), Aaron Klug (1985), César Milstein (1989), Sydney Brenner (1991), Hugh Huxley (1997) and John Walker (2012) as well as LMB alumni James Watson (1993) and John Gurdon (2003).
The Medical Research Council has been at the forefront of scientific discovery to improve human health. Founded in 1913 to tackle tuberculosis, the MRC now invests taxpayers’ money in some of the best medical research in the world across every area of health.